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Database: UniProt
Entry: A0A0R1JBC4_9LACO
LinkDB: A0A0R1JBC4_9LACO
Original site: A0A0R1JBC4_9LACO 
ID   A0A0R1JBC4_9LACO        Unreviewed;       375 AA.
AC   A0A0R1JBC4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-OCT-2025, entry version 34.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:KRK64503.1};
GN   ORFNames=FC72_GL000387 {ECO:0000313|EMBL:KRK64503.1};
OS   Companilactobacillus tucceti DSM 20183.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423811 {ECO:0000313|EMBL:KRK64503.1, ECO:0000313|Proteomes:UP000050929};
RN   [1] {ECO:0000313|EMBL:KRK64503.1, ECO:0000313|Proteomes:UP000050929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20183 {ECO:0000313|EMBL:KRK64503.1,
RC   ECO:0000313|Proteomes:UP000050929};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Genome Announc. 6:8322-8322(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRK64503.1}.
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DR   EMBL; AZDG01000011; KRK64503.1; -; Genomic_DNA.
DR   RefSeq; WP_057765849.1; NZ_AZDG01000011.1.
DR   AlphaFoldDB; A0A0R1JBC4; -.
DR   STRING; 1423811.FC72_GL000387; -.
DR   PATRIC; fig|1423811.3.peg.388; -.
DR   OrthoDB; 9796020at2; -.
DR   Proteomes; UP000050929; Unassembled WGS sequence.
DR   GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR020043; Deacetylase_Atu3266-like.
DR   InterPro; IPR047601; EF_0837-like.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03583; EF_0837; 1.
DR   NCBIfam; NF006689; PRK09237.1; 1.
DR   PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR   PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR   Pfam; PF22647; EF_0837-like_N; 1.
DR   PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050929};
KW   Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT   SITE            155
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT   MOD_RES         153
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ   SEQUENCE   375 AA;  41588 MW;  AE246C7AD7D664D2 CRC64;
     MVDLYVKNGK TITGQSIEVL IDQGKIIDVA TKIPGNVEAK KVFDLHSKYY VSSGWIDDHV
     HCYEKLSLYY DKPDLDGVDA GVTTVIDAGS TGYDNLPDFY KLSKNARTNV YAMCNISKTG
     IIAQDELGDM TRIKDDLVTK MIEEYSEFVV GIKARISKSV VSGNGVHPLE RAKAIQKLNH
     DLPLMVHIGS NPPELSEIMS LMSPGDIMTH CYNGKQNGIM NLDLHRIKDF AIEGYNRGII
     FDVGHGTDSF NFEVAQEARS IGLTPKSISS DLYHHNRENG PVYNLATCLD KMLYLGYTLP
     DILPMITTNP AENFNLKNKG QLKSGFDGDL TIFDVESKSK VLIDSNGNEK TTDMSIVPHF
     AVVAGEVYET NLEEF
//
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